2k7v

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{{Seed}}
 
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[[Image:2k7v.png|left|200px]]
 
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==Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form==
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The line below this paragraph, containing "STRUCTURE_2k7v", creates the "Structure Box" on the page.
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<StructureSection load='2k7v' size='340' side='right'caption='[[2k7v]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2k7v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7v OCA], [https://pdbe.org/2k7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7v RCSB], [https://www.ebi.ac.uk/pdbsum/2k7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7v ProSAT]</span></td></tr>
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{{STRUCTURE_2k7v| PDB=2k7v | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ODP2_ECOLI ODP2_ECOLI] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k7v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A prominent surface loop links the first two beta strands of the lipoyl domain (E2plip) from the pyruvate dehydrogenase multienzyme complex of Escherichia coli. We show here that shortening this loop by two residues generates a protein that populates two structurally distinct stable conformers: an active, native-like monomer (HM) and a functionally compromised misfolded dimer (LM). Conversion of LM to HM was observed after exposure to temperatures above 50 degrees C. Removal of two additional residues from the loop caused the protein to adopt exclusively the misfolded conformation. Detailed NMR structural studies of the misfolded dimer reveal that the N-terminal half of the domain was unfolded and dynamic, whereas the C-terminal halves of two monomers had associated to form a structure with two-fold symmetry and a topology mimicking that of the folded monomer. The surface loop is therefore a hitherto unsuspected determinant in the folding process that leads to a functional protein.
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===Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form===
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A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure.,Stott KM, Yusof AM, Perham RN, Jones DD Structure. 2009 Aug 12;17(8):1117-27. PMID:19679089<ref>PMID:19679089</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2k7v" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19679089}}, adds the Publication Abstract to the page
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*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19679089 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19679089}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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2K7V is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7V OCA].
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[[Category: Large Structures]]
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[[Category: Jones DD]]
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==Reference==
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[[Category: Perham RN]]
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<ref group="xtra">PMID:19679089</ref><references group="xtra"/>
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[[Category: Stott KM]]
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[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
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[[Category: Yusof AM]]
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[[Category: Escherichia coli]]
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[[Category: Jones, D D.]]
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[[Category: Perham, R N.]]
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[[Category: Stott, K M.]]
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[[Category: Yusof, A M.]]
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[[Category: Acyltransferase]]
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[[Category: Glycolysis]]
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[[Category: Lipoyl]]
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[[Category: Misfolded dimer]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 23 08:11:25 2009''
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Current revision

Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form

PDB ID 2k7v

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